Poly(Leu-Lys-Lys-Leu) and poly(Leu-Lys) are sequential amphiphilic peptide isomers that adopt respectively an ␣-helical conformation and a -sheet structure in saline solutions and at the air/water interface. The surface active properties of LKKL and LK sequential isopeptides containing 16, 20, and
Comparative interaction of α-helical and β-sheet amphiphilic isopeptides with phospholipid monolayers
✍ Scribed by Régine Maget-Dana; Dominique Lelièvre
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2001
- Tongue
- English
- Weight
- 194 KB
- Volume
- 59
- Category
- Article
- ISSN
- 0006-3525
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📜 SIMILAR VOLUMES
It was previously found that a cationic amphiphilic peptide, Ac-(Leu-Ala-Arg-Leu) 3 -NHCH 3 (4 3 ), caused the destabilization of a phospholipid membrane and showed strong antibacterial activity [Lee et al. Biochim. Biophys. Acta 1986; 862: 211 -219]. In order to investigate the effect of changing h
## Synopsis Configuration partition functions that describe the intramolecular formation of antiparallel /?-sheets and clusters of antiparallel interacting a-helices are very nearly of the same form. They can be interconverted by a simple change in notation and the addition of one weighting factor